3RNY

Crystal structure of human RSK1 C-terminal kinase domain

Summary for 3RNY

• Entry DOI: 10.2210/pdb3rny/pdb
• Descriptor: Ribosomal protein S6 kinase alpha-1, SODIUM ION (3 entities in total)
• Functional Keywords: protein kinase, autoinhibition, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q15418
• Total number of polymer chains: 2
• Total formula weight: 77690.69

Authors

Li, D.,Fu, T.-M.,Nan, J.,Su, X.-D. (deposition date: 2011-04-24, release date: 2012-04-25, Last modification date: 2023-09-13)

Primary citation

Li, D.,Fu, T.M.,Nan, J.,Liu, C.,Li, L.F.,Su, X.D.
Structural basis for the autoinhibition of the C-terminal kinase domain of human RSK1.
Acta Crystallogr.,Sect.D, 68:680-685, 2012

PubMed Abstract: p90 ribosomal S6 kinases (RSKs) respond to various mitogen stimuli and comprise two distinct protein kinase domains. The C-terminal kinase domain (CTKD) receives signal from ERK1/2 and adopts an autoinhibitory mechanism. Here, the crystal structure of human RSK1 CTKD is reported at 2.7 Å resolution. The structure shows a standard kinase fold, with the catalytic residues in the ATP-binding cleft orientated in optimal conformations for phosphotransfer. The inactivation of the CTKD is conferred by an extra α-helix (αL), which occupies the substrate-binding groove. In combination with previous knowledge, this structure indicates that activation of RSK1 involves the removal of αL from the substrate-binding groove induced by ERK1/2 phosphorylation.

PubMed: 22683790
DOI: 10.1107/S0907444912007457

Experimental method

X-RAY DIFFRACTION (2.7 Å)